GPV_MOUSE
ID GPV_MOUSE Reviewed; 567 AA.
AC O08742;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Platelet glycoprotein V;
DE Short=GPV;
DE AltName: Full=Glycoprotein 5;
DE AltName: CD_antigen=CD42d;
DE Flags: Precursor;
GN Name=Gp5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=9129030;
RA Ravanat C., Morales M., Azorsa D.O., Moog S., Schuhler S., Grunert P.,
RA Loew D., van Dorsselaer A., Cazenave J.-P., Lanza F.;
RT "Gene cloning of rat and mouse platelet glycoprotein V: identification of
RT megakaryocyte-specific promoters and demonstration of functional thrombin
RT cleavage.";
RL Blood 89:3253-3262(1997).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: The GPIb-V-IX complex functions as the vWF receptor and
CC mediates vWF-dependent platelet adhesion to blood vessels. The adhesion
CC of platelets to injured vascular surfaces in the arterial circulation
CC is a critical initiating event in hemostasis (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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DR EMBL; Z69595; CAA93441.1; -; Genomic_DNA.
DR CCDS; CCDS28100.1; -.
DR AlphaFoldDB; O08742; -.
DR SMR; O08742; -.
DR ComplexPortal; CPX-115; Glycoprotein Ib-IX-V complex.
DR ComplexPortal; CPX-118; Glycoprotein Ib-IX-V-Filamin-A complex.
DR STRING; 10090.ENSMUSP00000051895; -.
DR GlyGen; O08742; 7 sites.
DR PhosphoSitePlus; O08742; -.
DR CPTAC; non-CPTAC-3306; -.
DR MaxQB; O08742; -.
DR PaxDb; O08742; -.
DR PeptideAtlas; O08742; -.
DR PRIDE; O08742; -.
DR ProteomicsDB; 271083; -.
DR MGI; MGI:1096363; Gp5.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; O08742; -.
DR PhylomeDB; O08742; -.
DR Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-430116; GP1b-IX-V activation signalling.
DR Reactome; R-MMU-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-MMU-76009; Platelet Aggregation (Plug Formation).
DR PRO; PR:O08742; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O08742; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1990779; C:glycoprotein Ib-IX-V complex; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; IDA:MGI.
DR GO; GO:0007596; P:blood coagulation; IDA:ComplexPortal.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; ISO:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR GO; GO:0035855; P:megakaryocyte development; IMP:ComplexPortal.
DR GO; GO:0010544; P:negative regulation of platelet activation; IMP:MGI.
DR GO; GO:0030168; P:platelet activation; IMP:MGI.
DR GO; GO:0010572; P:positive regulation of platelet activation; ISO:MGI.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:MGI.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 4.
DR SMART; SM00369; LRR_TYP; 14.
DR SMART; SM00082; LRRCT; 1.
DR PROSITE; PS51450; LRR; 12.
PE 1: Evidence at protein level;
KW Blood coagulation; Cell adhesion; Glycoprotein; Hemostasis;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..567
FT /note="Platelet glycoprotein V"
FT /id="PRO_0000021362"
FT TOPO_DOM 17..522
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..50
FT /note="LRRNT"
FT REPEAT 75..96
FT /note="LRR 1"
FT REPEAT 99..120
FT /note="LRR 2"
FT REPEAT 123..144
FT /note="LRR 3"
FT REPEAT 147..168
FT /note="LRR 4"
FT REPEAT 171..193
FT /note="LRR 5"
FT REPEAT 195..216
FT /note="LRR 6"
FT REPEAT 219..240
FT /note="LRR 7"
FT REPEAT 243..264
FT /note="LRR 8"
FT REPEAT 267..288
FT /note="LRR 9"
FT REPEAT 291..312
FT /note="LRR 10"
FT REPEAT 315..337
FT /note="LRR 11"
FT REPEAT 340..361
FT /note="LRR 12"
FT REPEAT 364..385
FT /note="LRR 13"
FT REPEAT 388..409
FT /note="LRR 14"
FT DOMAIN 421..474
FT /note="LRRCT"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 567 AA; 63468 MW; C48643AA73967A7D CRC64;
MLRSALLSAV LPLLRAQPFP CPKTCKCVVR DAAQCSGGSV AHIAELGLPT NLTHILLFRM
DQGILRNHSF SGMTVLQRQM LSDSHISAID PGTFNDLVKL KTLRLTRNKI SRLPRAILDK
MVLLEQLFLD HNALRDLDQN LFQQLRNLQE LGLNQNQLSF LPANLFSSLR ELKLLDLSRN
NLTHLPKGLL GAQVKLEKLL LYSNQLTSVD SGLLSNLGAL TELRLERNHL RSVAPGAFDR
LGNLSSLTLS GNLLESLPPA LFLHVSSVSR LTLFENPLEE LPDVLFGEMA GLRELWLNGT
HLSTLPAAAF RNLSGLQTLG LTRNPRLSAL PRGVFQGLRE LRVLGLHTNA LAELRDDALR
GLGHLRQVSL RHNRLRALPR TLFRNLSSLE SVQLEHNQLE TLPGDVFAAL PQLTQVLLGH
NPWLCDCGLW RFLQWLRHHP DILGRDEPPQ CRGPEPRASL SFWELLQGDP WCPDPRSLPL
DPPTENALEA PVPSWLPNSW QSQTWAQLVA RGESPNNRLY WGLYILLLVA QAIIAAFIVF
AMIKIGQLFR TLIREKLLLE AMGKSCN
